5DDO
Structural and Dynamic Basis for Low Affinity-High Selectivity Binding of L-glutamine by the Gln-riboswitch
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 24-ID-E |
| Synchrotron site | APS |
| Beamline | 24-ID-E |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2013-01-01 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.9792 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 80.840, 99.652, 88.461 |
| Unit cell angles | 90.00, 99.05, 90.00 |
Refinement procedure
| Resolution | 39.917 - 3.100 |
| R-factor | 0.2305 |
| Rwork | 0.227 |
| R-free | 0.28870 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | U1A protein |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.261 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.7.3_928) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 3.210 |
| High resolution limit [Å] | 3.100 | 3.100 |
| Rmerge | 0.088 | 0.479 |
| Number of reflections | 12813 | |
| <I/σ(I)> | 15.7 | 2.5 |
| Completeness [%] | 99.7 | 99.5 |
| Redundancy | 4.1 | 2.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | EVAPORATION | 293 | 0.2 M Na-formate, 21% (w/v) PEG3350 |
